5HXO

Crystal Structure of Z,Z-Farnesyl Diphosphate Synthase with D71M, E75A and H103Y Mutants

Summary for 5HXO

• Entry DOI: 10.2210/pdb5hxo/pdb
• Related: 5HXN 5HXP 5HXQ 5HXT
• Descriptor: (2Z,6Z)-farnesyl diphosphate synthase, chloroplastic (2 entities in total)
• Functional Keywords: prenyltransferase, transferase
• Biological source: Solanum habrochaites (Wild tomato)
• Total number of polymer chains: 1
• Total formula weight: 26783.75

Authors

Lee, C.C.,Chan, Y.T.,Wang, A.H.J. (deposition date: 2016-01-31, release date: 2017-04-05, Last modification date: 2023-11-08)

Primary citation

Chan, Y.T.,Ko, T.P.,Yao, S.H.,Chen, Y.W.,Lee, C.C.,Wang, A.H.
Crystal Structure and Potential Head-to-Middle Condensation Function of aZ,Z-Farnesyl Diphosphate Synthase.
Acs Omega, 2:930-936, 2017

PubMed Abstract: Plants produce a wide variety of secondary metabolites in response to adverse environmental factors. ,-Farnesyl diphosphate (,-FPP), synthesized by ,-farnesyl diphosphate synthase (FPS), supports the formation of phytochemicals in wild tomatoes. Here, the crystal structure of N-terminal truncated FPS (ΔFPS) was determined. Irregular products including lavandulyl diphosphate and an unknown compound were surprisingly found. Apart from the truncated N-terminus as a functional regulator, structure-based analysis and mutagenesis assays revealed a residue H103 in ΔFPS as one of the key elements to this irregular function. A series of substrate-enzyme complex structures were obtained from ΔFPS-H103Y by co-crystallizing with isopentenyl diphosphate, dimethylallyl thiolodiphosphate, or both. Various substrate-binding modes were revealed. The catalytic mechanisms of both the head-to-tail and head-to-middle reactions in ΔFPS were proposed. Functional switch between the two mechanisms in this enzyme and the essential role played by the flexible C-terminus were elucidated as well.

PubMed: 30023621
DOI: 10.1021/acsomega.6b00562

Experimental method

X-RAY DIFFRACTION (2.05 Å)